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Database: UniProt
Entry: G9MJL0_HYPVG
LinkDB: G9MJL0_HYPVG
Original site: G9MJL0_HYPVG 
ID   G9MJL0_HYPVG            Unreviewed;       556 AA.
AC   G9MJL0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-MAY-2019, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHK25673.1};
GN   ORFNames=TRIVIDRAFT_31861 {ECO:0000313|EMBL:EHK25673.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK25673.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK25673.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A.,
RA   Antal Z., Atanasova L., Cervantes-Badillo M.G., Challacombe J.,
RA   Chertkov O., McCluskey K., Coulpier F., Deshpande N., von Doehren H.,
RA   Ebbole D.J., Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as
RT   the ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHK25673.1}.
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DR   EMBL; ABDF02000003; EHK25673.1; -; Genomic_DNA.
DR   RefSeq; XP_013959875.1; XM_014104400.1.
DR   SMR; G9MJL0; -.
DR   STRING; 29875.EHK25673; -.
DR   MEROPS; S53.010; -.
DR   EnsemblFungi; EHK25673; EHK25673; TRIVIDRAFT_31861.
DR   GeneID; 25793042; -.
DR   InParanoid; G9MJL0; -.
DR   OMA; DGKNTTR; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007115};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    556       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003523656.
FT   DOMAIN      170    556       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    246    246       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    250    250       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    462    462       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       504    504       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       505    505       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       536    536       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       538    538       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   556 AA;  60742 MW;  AC2DEE9E25AB23AF CRC64;
     MKARLLFLAF NALAMATPMA KPPLGTLKGV QPIQSGKISI ALQPECRELL EQTLHYLSDP
     SSRRYGQYLG REEAKALLRP RQDSTDAVKG WLSQAGIPAI DIQSDGQFIN VQVMAEQARA
     LLGTGYNSTL GIQTIPISSL PKDIESHVMT IHYAPTRTEM VTDWEECKSR ITPNCLKKLY
     HVDGYRARHV NKNRFGIVGF TGQAAQYDQL SAFLDDFAPY AANANFSVES VNGGENPQGR
     NEPTGEANVD IQYAVSMAYD VPVRFYATGG ANHDIIPDLD LSDTDNQALE PYLEFASHLL
     SLDDDELPKV VSISYGANEQ LFPRSYAQQV CDMFGQLGTR GVSIVVASGN LGPGVSCQSN
     DGTKRPKFMP SFPATCPYVT SVGATYGINP EIAVNFSSGG FSDYFIRPQW QDEAIEGYLK
     LHGREWKGYY NPHGRGFPDV AAQGVNYRFW SHGNEDSASG TSVSSPVFAA LIALLNDNRT
     KNGLPSMGFL NPWIYSIGSH AFTDITESKS LGCSGRSVIG LESPVIPNAG WDAVPGWDPV
     TGWGTPLFDR LMNLSY
//
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